1pwt Summary

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THERMODYNAMIC ANALYSIS OF ALPHA-SPECTRIN SH3 AND TWO OF ITS CIRCULAR PERMUTANTS WITH DIFFERENT LOOP LENGTHS: DISCERNING THE REASONS FOR RAPID FOLDING IN PROTEINS

The structure was published by Martinez, J.C., Viguera, A.R., Berisio, R., et al., Mateo, P.L., Filimonov, V.V., and Serrano, L., in 1999 in a paper entitled "Thermodynamic analysis of alpha-spectrin SH3 and two of its circular permutants with different loop lengths: discerning the reasons for rapid folding in proteins." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.77 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of ALPHA SPECTRIN. This molecule has the UniProt identifier P07751 (SPTN1_CHICK)search. The sample contained 61 residues which is < 90% of the natural sequence. Out of 61 residues 61 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A ALPHA SPECTRIN P07751 (967-1025) (SPTN1_CHICK)search Gallus gallussearch < 90% 61 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07751 (967 - 1025) ALPHA SPECTRIN Gallus gallus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A SH3-domainsearch SH3 Domainssearch SH3 domainsearch, Spectrin repeatsearch

Chain ID Biological process (GO)
A (P07751) endocytosissearch

Chain InterPro annotation
A SH3 domainsearch Spectrin alpha chain, SH3 domainsearch Endophilin-Asearch